Steroid hormone transforming aldo–keto reductases and cancer

Maintenance of Intratumoral Androgens in Metastatic Prostate Cancer: A Mechanism for Castration-Resistant Tumor Growth

Montgomery, R. B., Mostaghel, E. A., Vessella, R., Hess, D. L., Kalhorn, T. F., Higano, C. S., True, L. D., & Nelson, P. S. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0249 · Cited by 1,419 · see citing works

Increased Expression of Genes Converting Adrenal Androgens to Testosterone in Androgen-Independent Prostate Cancer

Stanbrough, M., Bubley, G. J., Ross, K., Golub, T. R., Rubin, M. A., Penning, T. M., Febbo, P. G., & Balk, S. P. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4000 · Cited by 1,082 · see citing works

Phase I Clinical Trial of a Selective Inhibitor of CYP17, Abiraterone Acetate, Confirms That Castration-Resistant Prostate Cancer Commonly Remains Hormone Driven

Attard, G., Reid, A. H. M., Yap, T. A., Raynaud, F., Dowsett, M., Settatree, S., Barrett, M., Parker, C., Martins, V., Folkerd, E., et al. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2007.15.9749 · Cited by 903 · see citing works

Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1–AKR1C4) of the aldo–keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones

PENNING, T. M., BURCZYNSKI, M. E., JEZ, J. M., HUNG, C.-F., LIN, H.-K., MA, H., MOORE, M., PALACKAL, N., & RATNAM, K. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510067 · Cited by 649 · see citing works

Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones

PENNING, T. M., BURCZYNSKI, M. E., JEZ, J. M., HUNG, C.-F., LIN, H.-K., MA, H., MOORE, M., PALACKAL, N., & RATNAM, K. (2000) · Biochemical Journal · doi:10.1042/bj3510067 · Cited by 649 · see citing works

Comparative anatomy of the aldo–keto reductase superfamily

Jez, J. M., BENNETT, M. J., Schlegel, B. P., Lewis, M., & Penning, T. M. (1997) · Biochemical Journal · doi:10.1042/bj3260625 · Cited by 603 · see citing works

Intracrinology: Role of the family of 17 beta-hydroxysteroid dehydrogenases in human physiology and disease

Labrie, F., Luu-The, V, Lin, S., Simard, J., Labrie, C., El-Alfy, M., Pelletier, G., & Belanger, A. (2000) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0250001 · Cited by 278 · see citing works

Human Cytosolic 3α-Hydroxysteroid Dehydrogenases of the Aldo-keto Reductase Superfamily Display Significant 3β-Hydroxysteroid Dehydrogenase Activity

Steckelbroeck, S., Jin, Y., Gopishetty, S., Oyesanmi, B., & Penning, T. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313308200 · Cited by 270 · see citing works

The aldo-keto reductase (AKR) superfamily: an update

Jez, J. M., & Penning, T. M. (2001) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00295-7 · Cited by 239 · see citing works

Molecular genetics and pathophysiology of 17 beta-hydroxysteroid dehydrogenase 3 deficiency

Andersson, S., Geissler, W. M., Wu, L., Davis, D. L., Grumbach, M. M., New, M. I., Schwarz, H. P., Blethen, S. L., Mendonca, B. B., Bloise, W., et al. (1996) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.81.1.130 · Cited by 223 · see citing works

Expression and Characterization of Recombinant Type 2 3α-Hydroxysteroid Dehydrogenase (HSD) from Human Prostate: Demonstration of Bifunctional 3α/17β-HSD Activity and Cellular Distribution

Lin, H.-K., Jez, J. M., Schlegel, B. P., Peehl, D. M., Pachter, J. A., & Penning, T. M. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.13.0026 · Cited by 194 · see citing works

Identification of a Principal mRNA Species for Human 3 -Hydroxysteroid Dehydrogenase Isoform (AKR1C3) That Exhibits High Prostaglandin D2 11-Ketoreductase Activity

Matsuura, K., Shiraishi, H., Hara, A., Sato, K., Deyashiki, Y., Ninomiya, M., & Sakai, S. (1998) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022211 · Cited by 172 · see citing works

AKR1C1 and AKR1C3 may determine progesterone and estrogen ratios in endometrial cancer

Rižner, T. L., Šmuc, T., Rupreht, R., Šinkovec, J., & Penning, T. M. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.10.009 · Cited by 159 · see citing works

The aldo-keto reductase AKR1C3 is a novel suppressor of cell differentiation that provides a plausible target for the non-cyclooxygenase-dependent antineoplastic actions of nonsteroidal anti-inflammatory drugs.

Desmond, J. C., Mountford, J. C., Drayson, M. T., Walker, E. A., Hewison, M., Ride, J. P., Luong, Q. T., Hayden, R. E., Vanin, E. F., & Bunce, C. M. (2003) · PubMed · Cited by 150 · see citing works

An indomethacin analogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor of aldo-keto reductase 1C3 (type 2 3α-HSD, type 5 17β-HSD, and prostaglandin F synthase), a potential target for the treatment of hormone dependent and hormone independent malignancies

Byrns, M. C., Steckelbroeck, S., & Penning, T. M. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.09.008 · Cited by 145 · see citing works

The Androgen Derivative 5α-Androstane-3β,17β-Diol Inhibits Prostate Cancer Cell Migration Through Activation of the Estrogen Receptor β Subtype

Guerini, V., Sau, D., Scaccianoce, E., Rusmini, P., Ciana, P., Maggi, A. C., Martini, P. G. V., Katzenellenbogen, B. S., Martini, L., Motta, M., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-1941 · Cited by 139 · see citing works

Human type 3 3α-hydroxysteroid dehydrogenase (aldo-keto reductase 1C2) and androgen metabolism in prostate cells

Rižner, T. L., Lin, H. K., Peehl, D. M., Steckelbroeck, S., Bauman, D. R., & Penning, T. M. (2003) · Endocrinology · doi:10.1210/en.2002-0032 · Cited by 132 · see citing works

Increased expression of type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase (AKR1C3) and its relationship with androgen receptor in prostate carcinoma

Fung, K.-M., Samara, E. N. S., Wong, C., Metwalli, A., Krlin, R., Bane, B., Liu, C. Z., Yang, J. T., Pitha, J. V., Culkin, D. J., et al. (2006) · Endocrine Related Cancer · doi:10.1677/erc.1.01048 · Cited by 129 · see citing works

Aldo-keto reductase (AKR) 1C3: Role in prostate disease and the development of specific inhibitors

Penning, T. M., Steckelbroeck, S., Bauman, D. R., Miller, M. W., Jin, Y., Peehl, D. M., Fung, K.-M. A., & Lin, H.-K. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.12.009 · Cited by 125 · see citing works

Development of Nonsteroidal Anti-Inflammatory Drug Analogs and Steroid Carboxylates Selective for Human Aldo-Keto Reductase Isoforms: Potential Antineoplastic Agents That Work Independently of Cyclooxygenase Isozymes

Bauman, D. R., Rudnick, S. I., Szewczuk, L. M., Jin, Y., Gopishetty, S. R., & Penning, T. M. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.006569 · Cited by 124 · see citing works

17β-Hydroxysteroid Dehydrogenase Type 1 Is an Independent Prognostic Marker in Breast Cancer

Oduwole, O. O., Yan, L., ISOMAA, V. V., Mäntyniemi, A., Pulkka, A. E., Soini, Y., & Vihko, P. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0446 · Cited by 117 · see citing works

Steroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3α-hydroxysteroid/dihydrodiol dehydrogenase

Bennett, M. J., Albert, R. H., Jez, J. M., Ma, H., Penning, T. M., & Lewis, M. (1997) · Structure · doi:10.1016/s0969-2126(97)00234-7 · Cited by 117 · see citing works

Characterization of a monoclonal antibody for human aldo-keto reductase AKR1C3 (type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase); immunohistochemical detection in breast and prostate

Lin, H., Steckelbroeck, S., Fung, K.-M. A., Jones, A. N., & Penning, T. M. (2004) · Steroids · doi:10.1016/j.steroids.2004.09.014 · Cited by 111 · see citing works

Crystal Structure of Human Prostaglandin F Synthase (AKR1C3),

Komoto, J., Yamada, T., Watanabe, K., & Takusagawa, F. (2004) · Biochemistry · doi:10.1021/bi036046x · Cited by 109 · see citing works

Crystal Structure of Human Type III 3α-Hydroxysteroid Dehydrogenase/Bile Acid Binding Protein Complexed with NADP+ and Ursodeoxycholate,

Jin, Y., Stayrook, S. E., Albert, R. H., Palackal, N. T., Penning, T. M., & Lewis, M. (2001) · Biochemistry · doi:10.1021/bi010919a · Cited by 99 · see citing works

Intracrinology of estrogens and androgens in breast carcinoma

Sasano, H., Suzuki, T., Miki, Y., & Moriya, T. (2007) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2007.09.012 · Cited by 93 · see citing works

In situ androgen producing enzymes in human prostate cancer

Nakamura, Y., Suzuki, T., Nakabayashi, M., et al. (2005) · Endocrine Related Cancer · doi:10.1677/erc.1.00914 · Cited by 89 · see citing works

Selective reduction of AKR1C2 in prostate cancer and its role in DHT metabolism

Ji, Q., Chang, L., Vandenberg, D. J., Stanczyk, F. Z., & Stolz, A. (2003) · The Prostate · doi:10.1002/pros.10192 · Cited by 85 · see citing works

Inhibition of a major NAD(P)-linked oxidoreductase from rat liver cytosol by steroidal and nonsteroidal anti-inflammatory agents and by prostaglandins.

Penning, T. M., & Talalay, P. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.14.4504 · Cited by 84 · see citing works

17β-Hydroxysteroid Dehydrogenase 14 Affects Estradiol Levels in Breast Cancer Cells and Is a Prognostic Marker in Estrogen Receptor–Positive Breast Cancer

Jansson, A., Gunnarsson, C., Cohen, M., Sivik, T., & Stål, O. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1448 · Cited by 73 · see citing works

Transcript Profiling of the Androgen Signal in Normal Prostate, Benign Prostatic Hyperplasia, and Prostate Cancer

Bauman, D. R., Steckelbroeck, S., Peehl, D. M., & Penning, T. M. (2006) · Endocrinology · doi:10.1210/en.2006-0627 · Cited by 71 · see citing works

Effect of androstenedione on growth of untransfected and aromatase-transfected MCF-7 cells in culture

Santner, S. J., Chen, S., Zhou, D., Korsunsky, Z., Martel, J., & Santen, R. J. (1993) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(93)90267-z · Cited by 66 · see citing works

Selective estrogen modulators as an anticancer tool: mechanisms of efficiency and resistance.

Sengupta, S., & Jordan, V. (2008) · Advances in Experimental Medicine and Biology · doi:10.1007/978-0-387-78818-0_13 · Cited by 60 · see citing works

Multiple steps determine the overall rate of the reduction of 5α-dihydrotestosterone catalyzed by human type 3 3α-hydroxysteroid dehydrogenase: implications for the elimination of androgens

Jin, Y., & Penning, T. M. (2006) · Biochemistry · doi:10.1021/bi060591r · Cited by 60 · see citing works

Molecular genetics and pathophysiology of 17 beta-hydroxysteroid dehydrogenase 3 deficiency.

Andersson, S., Geissler, W. M., Wu, L., et al. (1996) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.81.1.8550739 · Cited by 59 · see citing works

Elucidation of a Complete Kinetic Mechanism for a Mammalian Hydroxysteroid Dehydrogenase (HSD) and Identification of All Enzyme Forms on the Reaction Coordinate

Cooper, W. C., Jin, Y., & Penning, T. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703414200 · Cited by 58 · see citing works

Synthesis of prostaglandin F ethanolamide by prostaglandin F synthase and identification of Bimatoprost as a potent inhibitor of the enzyme: new enzyme assay method using LC/ESI/MS

Koda, N., Tsutsui, Y., Niwa, H., Ito, S., Woodward, D. F., & Watanabe, K. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.02.009 · Cited by 54 · see citing works

The molecular biology of androgenic 17β-hydroxysteroid dehydrogenases

Andersson, S., Geissler, W. M., Patel, S., & Wu, L. (1995) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(95)00039-3 · Cited by 54 · see citing works

Prostate Cancer Cells Increase Androgen Sensitivity by Increase in Nuclear Androgen Receptor and Androgen Receptor Coactivators; A Possible Mechanism of Hormone-Resistance of Prostate Cancer Cells

Fujimoto, N., Miyamoto, H., Mizokami, A., Harada, S., Nomura, M. J., Ueta, Y., Sasaguri, T., & Matsumoto, T. (2007) · Cancer Investigation · doi:10.1080/07357900601130698 · Cited by 49 · see citing works

Immunoelectron microscopic localization of 3beta-hydroxysteroid dehydrogenase and type 5 17beta-hydroxysteroid dehydrogenase in the human prostate and mammary gland

Pelletier, G., Luu-The, V., Elalfy, M., Li, S., & Labrie, F. (2001) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0260011 · Cited by 49 · see citing works

Targeted Chiral Lipidomics Analysis by Liquid Chromatography Electron Capture Atmospheric Pressure Chemical Ionization Mass Spectrometry (LC‐ECAPCI/MS)

Lee, S. H., & Blair, I. A. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)33009-7 · Cited by 39 · see citing works

Aromatase and COX in breast cancer: Enzyme inhibitors and beyond

Brueggemeier, R. W., Su, B., Sugimoto, Y., et al. (2007) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2007.05.021 · Cited by 34 · see citing works

Amplification of HSD17B1 has prognostic significance in postmenopausal breast cancer

Gunnarsson, C., Jerevall, P.-L., Hammar, K., Olsson, B., Nordenskjöld, B. A., Jansson, A., & Stål, O. (2007) · Breast Cancer Research and Treatment · doi:10.1007/s10549-007-9579-7 · Cited by 34 · see citing works

Suppression of aromatase in human breast cells by a cyclooxygenase-2 inhibitor and its analog involves multiple mechanisms independent of cyclooxygenase-2 inhibition

Su, B., Díaz‐Cruz, E. S., Landini, S., & Brueggemeier, R. W. (2007) · Steroids · doi:10.1016/j.steroids.2007.09.011 · Cited by 26 · see citing works

Mutation of Nicotinamide Pocket Residues in Rat Liver 3α-Hydroxysteroid Dehydrogenase Reveals Different Modes of Cofactor Binding

Ma, H., Ratnam, K., & Penning, T. M. (1999) · Biochemistry · doi:10.1021/bi991659o · Cited by 25 · see citing works

Exploiting the apoptotic actions of oestrogen to reverse antihormonal drug resistance in oestrogen receptor positive breast cancer patients

Jordan, V. C., Lewis-Wambi, J. S., Kim, H., Cunliffe, H. E., Ariazi, E. A., Sharma, C. G. N., Shupp, H. A., & Swaby, R. F. (2007) · The Breast · doi:10.1016/j.breast.2007.07.020 · Cited by 23 · see citing works

["Intracrinology". Autonomy and freedom of peripheral tissues].

Labrie, F., Bèlanger, A., Simard, J., Luu-The, V., & Labrie, C. (1995) · PubMed · Cited by 16 · see citing works

Development of selective androgen receptor modulators (SARMs)

Narayanan, R., Coss, C. C., & Dalton, J. T. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.06.013 · Cited by 251 · see citing works

Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism

Rižner, T. L., & Penning, T. M. (2014) · Steroids · doi:10.1016/j.steroids.2013.10.012 · Cited by 217 · see citing works

17β-Hydroxysteroid dehydrogenases (17β-HSDs) as therapeutic targets: Protein structures, functions, and recent progress in inhibitor development

Marchais-Oberwinkler, S., Henn, C., Möller, G., Klein, T., Negri, M., Oster, A., Spadaro, A., Werth, R., Wetzel, M., Xu, K., et al. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.12.013 · Cited by 216 · see citing works

Thyroid hormone, thyroid hormone receptors, and cancer: a clinical perspective

Moeller, L. C., & Führer, D. (2013) · Endocrine-Related Cancer · doi:10.1530/erc-12-0219 · Cited by 184 · see citing works

11β-Hydroxyandrostenedione: downstream metabolism by 11βHSD, 17βHSD and SRD5A produces novel substrates in familiar pathways

Swart, A. C., & Storbeck, K.-H. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2014.12.009 · Cited by 68 · see citing works

Overexpression of aldo–keto reductase 1C3 (AKR1C3) in LNCaP cells diverts androgen metabolism towards testosterone resulting in resistance to the 5α-reductase inhibitor finasteride

Byrns, M. C., Mindnich, R., Duan, L., & Penning, T. M. (2012) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.12.012 · Cited by 60 · see citing works

Progestins as inhibitors of the human 20-ketosteroid reductases, AKR1C1 and AKR1C3

Beranič, N., Gobec, S., & Rižner, T. L. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.12.012 · Cited by 39 · see citing works

The role of aromatase in breast tumors

Reed, M. J. (1994) · Breast Cancer Research and Treatment · doi:10.1007/bf00682737 · Cited by 53 · see citing works

Impact of androgen/estrogen ratio: Lessons learned from the aromatase over-expression mice

Li, X., & Rahman, N. A. (2008) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2008.07.025 · Cited by 48 · see citing works

Homologous Androgen Receptor Up-Regulation in Osteoblastic Cells May Be Associated with Enhanced Functional Androgen Responsiveness

Wiren, K. M., Keenan, E. J., Zhang, X., Ramsey, B., & ORWOLL, E. S. (1999) · Endocrinology · doi:10.1210/endo.140.7.6753 · Cited by 34 · see citing works

THE PHYSIOPATHOLOGICAL ROLES OF ANDROGENS IN MOTONEURONS

Poletti, A. (2020) · Istituto Lombardo - Accademia di Scienze e Lettere - Incontri di Studio · doi:10.4081/incontri.2019.607

Androgen receptor: role in the female lower vertebrate reproduction

Guerriero, G., Prins, G., Birch, L. A., et al. (2010) · Experimental and Clinical Endocrinology & Diabetes · doi:10.1055/s-0030-1267011